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Eric Macia
Researcher at Harvard University
Publications - 10
Citations - 3671
Eric Macia is an academic researcher from Harvard University. The author has contributed to research in topics: Golgi apparatus & Clathrin. The author has an hindex of 9, co-authored 9 publications receiving 3376 citations. Previous affiliations of Eric Macia include Centre national de la recherche scientifique.
Papers
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Journal ArticleDOI
Dynasore, a Cell-Permeable Inhibitor of Dynamin
Eric Macia,Marcelo Ehrlich,Ramiro Massol,Emmanuel Boucrot,Christian Brunner,Tomas Kirchhausen +5 more
TL;DR: Dynamin acts at two steps during clathrin coat formation; GTP hydrolysis is probably needed at both steps; Dynasore acts as a potent inhibitor of endocytic pathways known to depend on dynamin by rapidly blocking coated vesicle formation within seconds of dynasore addition.
Journal ArticleDOI
Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi
Ying-Jie Wang,Jing Wang,Hui Qiao Sun,Manuel Martinez,Yu Xiao Sun,Eric Macia,Tomas Kirchhausen,Joseph P. Albanesi,Michael G. Roth,Helen L. Yin +9 more
TL;DR: It is proposed that PI4KIIalpha establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.
Book ChapterDOI
Use of dynasore, the small molecule inhibitor of dynamin, in the regulation of endocytosis.
TL;DR: A detailed synthesis protocol for dynasore is presented, and a series of experiments used to analyze the inhibitory effects of dyn asore on dynamin in vitro and to study the effects of Dynasore on endocytosis in cells are described.
Journal ArticleDOI
Crystal structure of the clathrin adaptor protein 1 core
Ekaterina E. Heldwein,Eric Macia,Jing Wang,Helen L. Yin,Tomas Kirchhausen,Stephen C. Harrison,Stephen C. Harrison +6 more
TL;DR: The crystal structure of the core of the AP-1 complex, which functions in the trans-Golgi network (TGN), is reported and it is shown that directed mutations of residues at a particular corner of the gamma chain prevent recruitment to the TGN in cells and diminish PI-4-P- dependent, but not Arf1-dependent, liposome binding in vitro.
Journal ArticleDOI
PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal.
Jing Wang,Hui Qiao Sun,Eric Macia,Tomas Kirchhausen,Hadiya Watson,Juan S. Bonifacino,Helen L. Yin +6 more
TL;DR: The results show that the dual roles of PI4P can promote specific GGA targeting and cargo recognition at the TGN and has a novel role in promoting their recognition of the ubiquitin (Ub) sorting signal.